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Journal of Pharmacology And Experimental Therapeutics Fast Forward
First published on April 27, 2005; DOI: 10.1124/jpet.105.084418

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*Compound via MeSH
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Hazardous Substances DB
*LEAD, ELEMENTAL
*ZINC COMPOUNDS
*ZINC, ELEMENTAL


Received for publication February 3, 2005.
Revised April 19, 2005.
Accepted for publication April 20, 2005.

Zinc activates TREK-2 potassium channel activity

Jin-Sung Kim 1, Jin-Yong Park 1, Ho-Won Kang 1, Eun-Jung Lee 1, Hyoweon Bang 2, Jung-Ha Lee 1*

1 Sogang University 2 Chung-Ang University

* Address correspondence to: E-mail: jhleem{at}ccs.sogang.ac.kr

Abstract

TREK-2 is thought to contribute to setting the resting membrane potential and to tuning action potential properties. In the present study, the effects of divalent metal ions (Ba2+, Co2+, Ni2+, Pb2+, and Zn2+) were examined on TREK-2 expressed in Xenopus oocytes using the two-electrode voltage clamping technique. Pb2+ inhibited TREK channel activity (IC50 = 15.6 µM), while Zn2+ enhanced it in a dose dependent manner (EC50 = 87.1 µM). Ba2+ slightly inhibited TREK currents, but only at high concentrations. Co2+ and Ni2+ had no significant effect. The structural element(s) contributing to the zinc enhancement effect were studied using a series of chimeras consisting of Zn2+-activated TREK-2 and Zn2+-inhibited TASK-3. The structural elements were localized to the first pore and the preceding extracellular loop of TREK-2, in which multiple residues including H121, H156, D158, and N177 are likely to be involved in the zinc activation effect. Stimulation by Zn2+ may be used as a criterion of TREK-2 distinguishing it from other two-pore K+ channels.


Key words: TASK-3, TREK-2, Two-electrode voltage clamping, lead, two-pore potassium channel, zinc


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